Vesicle transport protein SEC20 (BNIP1)
The protein contains 228 amino acids for an estimated molecular weight of 26132 Da.
As part of a SNARE complex may be involved in endoplasmic reticulum membranes fusion and be required for the maintenance of endoplasmic reticulum organization (PubMed:15272311). Plays also a role in apoptosis (PubMed:7954800, PubMed:15272311, PubMed:23896122). It is for instance required for endoplasmic reticulum stress-induced apoptosis (PubMed:23896122). As a substrate of RNF185 interacting with SQSTM1, might also be involved in mitochondrial autophagy (Probable). (updated: Nov. 7, 2018)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is predicted to be membranous by TOPCONS.
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| Variant | Description |
|---|---|
| dbSNP:rs5745100 |
Biological Process
Apoptotic process
Autophagy
Endoplasmic reticulum membrane fusion
Endoplasmic reticulum organization
Execution phase of apoptosis
Negative regulation of apoptotic process
Response to activity
Response to oxygen-glucose deprivation
Response to starvation
Retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum
Vesicle-mediated transport
Viral process
The reference OMIM entry for this protein is 603291
Bcl2/adenovirus e1b 19-kd protein-interacting protein 1; bnip1
Nip1
CLONING
Using a yeast 2-hybrid system to identify proteins that interact with discrete domains of the E1B 19-kD protein, which is involved in suppression of cell death, Boyd et al. (1994) cloned human B-cell cDNAs encoding NIP1, NIP2 (603292), and NIP3 (603293). The deduced NIP1 protein has 228 amino acids and contains a putative membrane-spanning hydrophobic domain. Although the authors found no significant sequence homology between NIP1 and other proteins, they identified a 59- to 83-amino acid region of NIP1 that shows 29% to 36% identity to a conserved region within the catalytic domain of 3 mammalian 3-prime-5-prime-cyclic nucleotide phosphodiesterases. Boyd et al. (1994) localized NIP1 to the nuclear envelope region and to other cytoplasmic structures.GENE FUNCTION
Adenovirus E1B 19-kD protein protects against cell death induced by viral infection and certain external stimuli. Using yeast 2-hybrid analysis, Boyd et al. (1994) showed that NIP1, NIP2, and NIP3 interacted with the adenovirus E1B 19-kD protein and with human BCL2 (151430), which can functionally substitute for the 19-kD protein during adenovirus infection. The interactions occurred at bipartite sequence motifs common to both the E1B 19-kD and BCL2 proteins.MAPPING
Gross (2012) mapped the BNIP1 gene to chromosome 5q35.1 based on an alignment of the BNIP1 sequence (GenBank GENBANK AF083956) with the genomic sequence (GRCh37). ... More on the omim web site
May 13, 2019: Protein entry updated
Automatic update: model status changed
Nov. 17, 2018: Protein entry updated
Automatic update: model status changed
Nov. 16, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Oct. 27, 2017: Protein entry updated
Automatic update: model status changed
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 603291 was added.
Feb. 25, 2016: Protein entry updated
Automatic update: model status changed
Feb. 24, 2016: Protein entry updated
Automatic update: model status changed
Jan. 25, 2016: Protein entry updated
Automatic update: model status changed